The related coactivator complexes SAGA and ATAC control embryonic stem cell self-renewal through acetyltransferase-independent mechanisms.
Animals
Cell Self Renewal
/ physiology
Embryonic Stem Cells
/ metabolism
Histone Acetyltransferases
/ metabolism
Histones
/ metabolism
Mice
Protein Processing, Post-Translational
/ physiology
RNA Polymerase II
/ metabolism
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ metabolism
Trans-Activators
/ metabolism
4sU labeling
ATAC
HAT-independent function
Pol II transcription
SAGA
coactivator complexes
histone acetyltransferase
mouse embryonic stem cells
newly synthesized RNA
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
24 08 2021
24 08 2021
Historique:
received:
27
01
2021
revised:
17
06
2021
accepted:
03
08
2021
entrez:
25
8
2021
pubmed:
26
8
2021
medline:
12
2
2022
Statut:
ppublish
Résumé
SAGA (Spt-Ada-Gcn5 acetyltransferase) and ATAC (Ada-two-A-containing) are two related coactivator complexes, sharing the same histone acetyltransferase (HAT) subunit. The HAT activities of SAGA and ATAC are required for metazoan development, but the role of these complexes in RNA polymerase II transcription is less understood. To determine whether SAGA and ATAC have redundant or specific functions, we compare the effects of HAT inactivation in each complex with that of inactivation of either SAGA or ATAC core subunits in mouse embryonic stem cells (ESCs). We show that core subunits of SAGA or ATAC are required for complex assembly and mouse ESC growth and self-renewal. Surprisingly, depletion of HAT module subunits causes a global decrease in histone H3K9 acetylation, but does not result in significant phenotypic or transcriptional defects. Thus, our results indicate that SAGA and ATAC are differentially required for self-renewal of mouse ESCs by regulating transcription through different pathways in a HAT-independent manner.
Identifiants
pubmed: 34433046
pii: S2211-1247(21)01036-6
doi: 10.1016/j.celrep.2021.109598
pmc: PMC8430043
mid: NIHMS1735653
pii:
doi:
Substances chimiques
Histones
0
Saccharomyces cerevisiae Proteins
0
Trans-Activators
0
Histone Acetyltransferases
EC 2.3.1.48
RNA Polymerase II
EC 2.7.7.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
109598Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM131626
Pays : United States
Informations de copyright
Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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